IMR Press / FBL / Volume 21 / Issue 2 / DOI: 10.2741/4394

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.


New insights into the activation, interaction partners and possible functions of MK5/PRAK

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1 Department of Medical Biology UiT-The Arctic University of Norway, N9037 Tromsoe, Norway
2 Department of Pharmacy, UiT-The Arctic University of Norway, N9037 Tromsoe, Norway
3 Cancer Research UK Stress Response Laboratory, Medical Research Institute, Division of Cancer Research, Jacqui Wood Cancer Centre, James Arrot Drive, Ninewells Hospital and Medical School, Dundee DD1 9SY, United Kingdom
Front. Biosci. (Landmark Ed) 2016, 21(2), 374–384;
Published: 1 January 2016

MAP kinase-activated protein kinase 5 (MK5) was first described as a downstream target of the p38 MAP kinase pathway leading to its alternative acronym of p38-regulated/activated protein kinase (PRAK). However, since the discovery that MK5 is a bona fide interaction partner of the atypical MAP kinases ERK3 and ERK4 and that this interaction leads to both the activation and subcellular relocalisation of MK5, there has been considerable debate as to the relative roles of these MAPK pathways in mediating the activation and biological functions of MK5. Here we discuss recent progress in defining novel upstream components of the ERK3/ERK4 signalling pathway, our increased understanding of the mechanism by which MK5 interacts with and is activated by ERK3 and ERK4, and the discovery of novel interaction partners for MK5. Finally, we review recent literature that suggests novel biological functions for MK5 in a range of physiological and pathophysiological conditions including neuronal function and cancer.

Protein kinases
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